Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion

Lloyd Hutchinson, Kim Goldsmith, Dan Snoddy, Hara Ghosh, Frank L. Graham, David Johnson

Research output: Contribution to journalArticle

102 Citations (Scopus)

Abstract

Antipeptide sera were used to identify a novel glycoprotein encoded by the UL53 gene of herpes simplex virus type 1 (HSV-1). The UL53 gene product is thought to play a central role in regulating membrane fusion because mutations giving rise to the syncytial phenotype, wherein cells are extensively fused, frequently map to this gene. A single 40-kDa protein, designated gK (the ninth HSV-1 glycoprotein to be described), was detected with antipeptide sera in cells infected with both wild-type and syncytial strains of HSV-1 which were labelled with [35S]methionine and [35S]cysteine or with [3H]glucosamine, and this protein was sensitive to treatment of cells with tunicamycin. With all other RSV glycoproteins studied to date, at least two glycosylated species, often differing substantially in electrophoretic mobility, have been observed in infected cells; thus, gK is unusual in this respect. The 40-kDa gK protein was also immunoprecipitated from cells infected with a recombinant adenovirus vector carrying the UL53 gene. Two glycosylated species of 39 and 41 kDa were produced when UL53 mRNA was translated in vitro in the presence of microsomes, and these proteins differed from gK produced in infected cells not only because they possessed different electrophoretic mobilities but also because they were unable to enter gels after being heated. In addition, a 36-kDa protein was detected in extracts from cells infected with HSV-2 with use of these sera.

Original languageEnglish (US)
Pages (from-to)5603-5609
Number of pages7
JournalJournal of Virology
Volume66
Issue number9
StatePublished - Sep 1992
Externally publishedYes

Fingerprint

herpes simplex
cell fusion
Cell Fusion
Simplexvirus
glycoproteins
Glycoproteins
viruses
Human herpesvirus 1
Human Herpesvirus 1
cells
Proteins
Genes
proteins
Serum
genes
Tunicamycin
Membrane Fusion
Human Herpesvirus 2
tunicamycin
Glucosamine

ASJC Scopus subject areas

  • Immunology

Cite this

Hutchinson, L., Goldsmith, K., Snoddy, D., Ghosh, H., Graham, F. L., & Johnson, D. (1992). Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion. Journal of Virology, 66(9), 5603-5609.

Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion. / Hutchinson, Lloyd; Goldsmith, Kim; Snoddy, Dan; Ghosh, Hara; Graham, Frank L.; Johnson, David.

In: Journal of Virology, Vol. 66, No. 9, 09.1992, p. 5603-5609.

Research output: Contribution to journalArticle

Hutchinson, L, Goldsmith, K, Snoddy, D, Ghosh, H, Graham, FL & Johnson, D 1992, 'Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion', Journal of Virology, vol. 66, no. 9, pp. 5603-5609.
Hutchinson, Lloyd ; Goldsmith, Kim ; Snoddy, Dan ; Ghosh, Hara ; Graham, Frank L. ; Johnson, David. / Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion. In: Journal of Virology. 1992 ; Vol. 66, No. 9. pp. 5603-5609.
@article{97ab5062ace94e0f8bb60f0d6924e54b,
title = "Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion",
abstract = "Antipeptide sera were used to identify a novel glycoprotein encoded by the UL53 gene of herpes simplex virus type 1 (HSV-1). The UL53 gene product is thought to play a central role in regulating membrane fusion because mutations giving rise to the syncytial phenotype, wherein cells are extensively fused, frequently map to this gene. A single 40-kDa protein, designated gK (the ninth HSV-1 glycoprotein to be described), was detected with antipeptide sera in cells infected with both wild-type and syncytial strains of HSV-1 which were labelled with [35S]methionine and [35S]cysteine or with [3H]glucosamine, and this protein was sensitive to treatment of cells with tunicamycin. With all other RSV glycoproteins studied to date, at least two glycosylated species, often differing substantially in electrophoretic mobility, have been observed in infected cells; thus, gK is unusual in this respect. The 40-kDa gK protein was also immunoprecipitated from cells infected with a recombinant adenovirus vector carrying the UL53 gene. Two glycosylated species of 39 and 41 kDa were produced when UL53 mRNA was translated in vitro in the presence of microsomes, and these proteins differed from gK produced in infected cells not only because they possessed different electrophoretic mobilities but also because they were unable to enter gels after being heated. In addition, a 36-kDa protein was detected in extracts from cells infected with HSV-2 with use of these sera.",
author = "Lloyd Hutchinson and Kim Goldsmith and Dan Snoddy and Hara Ghosh and Graham, {Frank L.} and David Johnson",
year = "1992",
month = "9",
language = "English (US)",
volume = "66",
pages = "5603--5609",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "9",

}

TY - JOUR

T1 - Identification and characterization of a novel Herpes simplex virus glycoprotein, gK, involved in cell fusion

AU - Hutchinson, Lloyd

AU - Goldsmith, Kim

AU - Snoddy, Dan

AU - Ghosh, Hara

AU - Graham, Frank L.

AU - Johnson, David

PY - 1992/9

Y1 - 1992/9

N2 - Antipeptide sera were used to identify a novel glycoprotein encoded by the UL53 gene of herpes simplex virus type 1 (HSV-1). The UL53 gene product is thought to play a central role in regulating membrane fusion because mutations giving rise to the syncytial phenotype, wherein cells are extensively fused, frequently map to this gene. A single 40-kDa protein, designated gK (the ninth HSV-1 glycoprotein to be described), was detected with antipeptide sera in cells infected with both wild-type and syncytial strains of HSV-1 which were labelled with [35S]methionine and [35S]cysteine or with [3H]glucosamine, and this protein was sensitive to treatment of cells with tunicamycin. With all other RSV glycoproteins studied to date, at least two glycosylated species, often differing substantially in electrophoretic mobility, have been observed in infected cells; thus, gK is unusual in this respect. The 40-kDa gK protein was also immunoprecipitated from cells infected with a recombinant adenovirus vector carrying the UL53 gene. Two glycosylated species of 39 and 41 kDa were produced when UL53 mRNA was translated in vitro in the presence of microsomes, and these proteins differed from gK produced in infected cells not only because they possessed different electrophoretic mobilities but also because they were unable to enter gels after being heated. In addition, a 36-kDa protein was detected in extracts from cells infected with HSV-2 with use of these sera.

AB - Antipeptide sera were used to identify a novel glycoprotein encoded by the UL53 gene of herpes simplex virus type 1 (HSV-1). The UL53 gene product is thought to play a central role in regulating membrane fusion because mutations giving rise to the syncytial phenotype, wherein cells are extensively fused, frequently map to this gene. A single 40-kDa protein, designated gK (the ninth HSV-1 glycoprotein to be described), was detected with antipeptide sera in cells infected with both wild-type and syncytial strains of HSV-1 which were labelled with [35S]methionine and [35S]cysteine or with [3H]glucosamine, and this protein was sensitive to treatment of cells with tunicamycin. With all other RSV glycoproteins studied to date, at least two glycosylated species, often differing substantially in electrophoretic mobility, have been observed in infected cells; thus, gK is unusual in this respect. The 40-kDa gK protein was also immunoprecipitated from cells infected with a recombinant adenovirus vector carrying the UL53 gene. Two glycosylated species of 39 and 41 kDa were produced when UL53 mRNA was translated in vitro in the presence of microsomes, and these proteins differed from gK produced in infected cells not only because they possessed different electrophoretic mobilities but also because they were unable to enter gels after being heated. In addition, a 36-kDa protein was detected in extracts from cells infected with HSV-2 with use of these sera.

UR - http://www.scopus.com/inward/record.url?scp=0026803324&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026803324&partnerID=8YFLogxK

M3 - Article

C2 - 1323714

AN - SCOPUS:0026803324

VL - 66

SP - 5603

EP - 5609

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 9

ER -